1om9
From Proteopedia
(New page: 200px<br /> <applet load="1om9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1om9, resolution 2.50Å" /> '''Structure of the GG...) |
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| - | [[Image:1om9. | + | [[Image:1om9.jpg|left|200px]]<br /><applet load="1om9" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1om9, resolution 2.50Å" /> | caption="1om9, resolution 2.50Å" /> | ||
'''Structure of the GGA1-appendage in complex with the p56 binding peptide'''<br /> | '''Structure of the GGA1-appendage in complex with the p56 binding peptide'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1OM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OM9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: gga]] | [[Category: gga]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:34:33 2008'' |
Revision as of 14:34, 15 February 2008
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Structure of the GGA1-appendage in complex with the p56 binding peptide
Overview
The Golgi-associated, gamma-adaptin-related, ADP-ribosylation-factor, binding proteins (GGAs) and adaptor protein (AP)-1 are adaptors involved, in clathrin-mediated transport between the trans-Golgi network and, endosomal system. The appendage domains of GGAs and the AP-1 gamma-adaptin, subunit are structurally homologous and have been proposed to bind to, accessory proteins via interaction with short sequences containing, phenylalanines and acidic residues. Here we present the structure of the, human GGA1 appendage in complex with its cognate binding peptide from the, p56 accessory protein (DDDDFGGFEAAETFD) as determined by X-ray, crystallography. The interaction is governed predominantly by packing of, the first two phenylalanine residues of the peptide with conserved basic, and hydrophobic residues from GGA1. Additionally, several main chain, hydrogen bonds cause the peptide to form an additional beta-strand on the, edge of the preexisting beta-sheet of the protein. Isothermal titration, calorimetry was used to assess the affinities of different peptides for, the GGA and gamma-appendage domains.
About this Structure
1OM9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for binding of accessory proteins by the appendage domain of GGAs., Collins BM, Praefcke GJ, Robinson MS, Owen DJ, Nat Struct Biol. 2003 Aug;10(8):607-13. PMID:12858163
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